DSN1_HUMAN
ID DSN1_HUMAN Reviewed; 356 AA.
AC Q9H410; B4DWT2; E1P5U9; Q5JW55; Q5JW56; Q9H8P4;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Kinetochore-associated protein DSN1 homolog;
GN Name=DSN1; Synonyms=C20orf172, MIS13;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC TISSUE=Esophageal carcinoma, Esophagus, Ovarian carcinoma, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, INTERACTION WITH MIS12; KNL1; CBX3; CBX5; NSL1 AND PMF1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15502821; DOI=10.1038/ncb1187;
RA Obuse C., Iwasaki O., Kiyomitsu T., Goshima G., Toyoda Y., Yanagida M.;
RT "A conserved Mis12 centromere complex is linked to heterochromatic HP1 and
RT outer kinetochore protein Zwint-1.";
RL Nat. Cell Biol. 6:1135-1141(2004).
RN [6]
RP FUNCTION, COMPONENT OF MIS12 COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=16585270; DOI=10.1083/jcb.200509158;
RA Kline S.L., Cheeseman I.M., Hori T., Fukagawa T., Desai A.;
RT "The human Mis12 complex is required for kinetochore assembly and proper
RT chromosome segregation.";
RL J. Cell Biol. 173:9-17(2006).
RN [7]
RP INTERACTION WITH KNL1.
RX PubMed=17981135; DOI=10.1016/j.devcel.2007.09.005;
RA Kiyomitsu T., Obuse C., Yanagida M.;
RT "Human Blinkin/AF15q14 is required for chromosome alignment and the mitotic
RT checkpoint through direct interaction with Bub1 and BubR1.";
RL Dev. Cell 13:663-676(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-30; SER-77 AND
RP SER-81, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-58 AND SER-81, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP INTERACTION WITH KNSTRN.
RX PubMed=23035123; DOI=10.1074/jbc.m112.406652;
RA Wang X., Zhuang X., Cao D., Chu Y., Yao P., Liu W., Liu L., Adams G.,
RA Fang G., Dou Z., Ding X., Huang Y., Wang D., Yao X.;
RT "Mitotic regulator SKAP forms a link between kinetochore core complex KMN
RT and dynamic spindle microtubules.";
RL J. Biol. Chem. 287:39380-39390(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-77; SER-81; SER-109;
RP SER-125 AND SER-331, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-253, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Part of the MIS12 complex which is required for normal
CC chromosome alignment and segregation and kinetochore formation during
CC mitosis. {ECO:0000269|PubMed:15502821, ECO:0000269|PubMed:16585270}.
CC -!- SUBUNIT: Component of the MIS12 complex composed of MIS12, DSN1, NSL1
CC and PMF1. Also interacts with KNL1, CBX3 and CBX5. Interacts with
CC KNSTRN. {ECO:0000269|PubMed:15502821, ECO:0000269|PubMed:17981135,
CC ECO:0000269|PubMed:23035123}.
CC -!- INTERACTION:
CC Q9H410; P24539: ATP5PB; NbExp=3; IntAct=EBI-1001144, EBI-1044810;
CC Q9H410; P46379-2: BAG6; NbExp=3; IntAct=EBI-1001144, EBI-10988864;
CC Q9H410; P21810: BGN; NbExp=3; IntAct=EBI-1001144, EBI-762076;
CC Q9H410; Q96A83-2: COL26A1; NbExp=3; IntAct=EBI-1001144, EBI-21553822;
CC Q9H410; O14964: HGS; NbExp=3; IntAct=EBI-1001144, EBI-740220;
CC Q9H410; Q9UMF0: ICAM5; NbExp=3; IntAct=EBI-1001144, EBI-6398041;
CC Q9H410; O14901: KLF11; NbExp=3; IntAct=EBI-1001144, EBI-948266;
CC Q9H410; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-1001144, EBI-2811583;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15502821,
CC ECO:0000269|PubMed:16585270}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:15502821, ECO:0000269|PubMed:16585270}.
CC Note=Associated with the kinetochore. {ECO:0000269|PubMed:15502821,
CC ECO:0000269|PubMed:16585270}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9H410-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H410-2; Sequence=VSP_003826;
CC Name=4;
CC IsoId=Q9H410-4; Sequence=VSP_044281;
CC Name=3;
CC IsoId=Q9H410-3; Sequence=VSP_043204;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14564.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK093031; BAC04024.1; -; mRNA.
DR EMBL; AK023408; BAB14564.1; ALT_FRAME; mRNA.
DR EMBL; AK301671; BAG63144.1; -; mRNA.
DR EMBL; AK301840; BAG63283.1; -; mRNA.
DR EMBL; AL132768; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW76101.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76102.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76104.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76106.1; -; Genomic_DNA.
DR EMBL; BC058899; AAH58899.1; -; mRNA.
DR CCDS; CCDS13286.1; -. [Q9H410-1]
DR CCDS; CCDS46596.1; -. [Q9H410-3]
DR CCDS; CCDS46597.1; -. [Q9H410-4]
DR RefSeq; NP_001138787.1; NM_001145315.1. [Q9H410-1]
DR RefSeq; NP_001138788.1; NM_001145316.1. [Q9H410-1]
DR RefSeq; NP_001138789.1; NM_001145317.1. [Q9H410-3]
DR RefSeq; NP_001138790.1; NM_001145318.1. [Q9H410-4]
DR RefSeq; NP_079194.3; NM_024918.3. [Q9H410-1]
DR RefSeq; XP_006723939.1; XM_006723876.2. [Q9H410-3]
DR PDB; 5LSI; X-ray; 2.00 A; D=68-200.
DR PDB; 5LSJ; X-ray; 3.25 A; D/F=186-356.
DR PDB; 5LSK; X-ray; 3.50 A; D=68-356.
DR PDBsum; 5LSI; -.
DR PDBsum; 5LSJ; -.
DR PDBsum; 5LSK; -.
DR AlphaFoldDB; Q9H410; -.
DR SMR; Q9H410; -.
DR BioGRID; 123045; 96.
DR ComplexPortal; CPX-5643; Kinetochore MIS12 complex.
DR CORUM; Q9H410; -.
DR IntAct; Q9H410; 63.
DR MINT; Q9H410; -.
DR STRING; 9606.ENSP00000389810; -.
DR GlyGen; Q9H410; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H410; -.
DR MetOSite; Q9H410; -.
DR PhosphoSitePlus; Q9H410; -.
DR BioMuta; DSN1; -.
DR DMDM; 28201793; -.
DR EPD; Q9H410; -.
DR jPOST; Q9H410; -.
DR MassIVE; Q9H410; -.
DR MaxQB; Q9H410; -.
DR PaxDb; Q9H410; -.
DR PeptideAtlas; Q9H410; -.
DR PRIDE; Q9H410; -.
DR ProteomicsDB; 5379; -.
DR ProteomicsDB; 80777; -. [Q9H410-1]
DR ProteomicsDB; 80778; -. [Q9H410-2]
DR ProteomicsDB; 80779; -. [Q9H410-3]
DR Antibodypedia; 1232; 186 antibodies from 26 providers.
DR DNASU; 79980; -.
DR Ensembl; ENST00000373734.8; ENSP00000362839.4; ENSG00000149636.16. [Q9H410-3]
DR Ensembl; ENST00000373750.9; ENSP00000362855.4; ENSG00000149636.16. [Q9H410-1]
DR Ensembl; ENST00000426836.5; ENSP00000389810.1; ENSG00000149636.16. [Q9H410-1]
DR Ensembl; ENST00000448110.6; ENSP00000404463.1; ENSG00000149636.16. [Q9H410-4]
DR GeneID; 79980; -.
DR KEGG; hsa:79980; -.
DR MANE-Select; ENST00000373750.9; ENSP00000362855.4; NM_001145315.2; NP_001138787.1.
DR UCSC; uc002xga.4; human. [Q9H410-1]
DR CTD; 79980; -.
DR DisGeNET; 79980; -.
DR GeneCards; DSN1; -.
DR HGNC; HGNC:16165; DSN1.
DR HPA; ENSG00000149636; Low tissue specificity.
DR MIM; 609175; gene.
DR neXtProt; NX_Q9H410; -.
DR OpenTargets; ENSG00000149636; -.
DR PharmGKB; PA162384106; -.
DR VEuPathDB; HostDB:ENSG00000149636; -.
DR eggNOG; ENOG502S0JV; Eukaryota.
DR GeneTree; ENSGT00390000011347; -.
DR HOGENOM; CLU_042801_0_0_1; -.
DR InParanoid; Q9H410; -.
DR OMA; KSQSWRR; -.
DR OrthoDB; 922920at2759; -.
DR PhylomeDB; Q9H410; -.
DR TreeFam; TF335504; -.
DR PathwayCommons; Q9H410; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q9H410; -.
DR SIGNOR; Q9H410; -.
DR BioGRID-ORCS; 79980; 672 hits in 1095 CRISPR screens.
DR ChiTaRS; DSN1; human.
DR GeneWiki; DSN1; -.
DR GenomeRNAi; 79980; -.
DR Pharos; Q9H410; Tbio.
DR PRO; PR:Q9H410; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9H410; protein.
DR Bgee; ENSG00000149636; Expressed in ventricular zone and 132 other tissues.
DR ExpressionAtlas; Q9H410; baseline and differential.
DR Genevisible; Q9H410; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0000776; C:kinetochore; IDA:WormBase.
DR GO; GO:0000444; C:MIS12/MIND type complex; IDA:UniProtKB.
DR GO; GO:0031617; C:NMS complex; IC:ComplexPortal.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0000818; C:nuclear MIS12/MIND complex; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR InterPro; IPR013218; Dsn1/Mis13.
DR PANTHER; PTHR14778; PTHR14778; 1.
DR Pfam; PF08202; MIS13; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Centromere;
KW Chromosome; Chromosome partition; Isopeptide bond; Kinetochore; Mitosis;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..356
FT /note="Kinetochore-associated protein DSN1 homolog"
FT /id="PRO_0000079481"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 253
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..84
FT /note="MTSVTRSEIIDEKGPVMSKTHDHQLESSLSPVEVFAKTSASLEMNQGVSEER
FT IHLGSSPKKGGNCDLSHQERLQSKSLHLSPQE -> MIINWNQVSVLWKCLLK (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_003826"
FT VAR_SEQ 1..16
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044281"
FT VAR_SEQ 12..118
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043204"
FT CONFLICT 142
FT /note="F -> S (in Ref. 1; BAC04024)"
FT /evidence="ECO:0000305"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:5LSI"
FT HELIX 130..149
FT /evidence="ECO:0007829|PDB:5LSI"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:5LSI"
FT HELIX 161..184
FT /evidence="ECO:0007829|PDB:5LSI"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:5LSI"
FT HELIX 204..242
FT /evidence="ECO:0007829|PDB:5LSJ"
FT HELIX 265..269
FT /evidence="ECO:0007829|PDB:5LSJ"
FT HELIX 274..314
FT /evidence="ECO:0007829|PDB:5LSJ"
SQ SEQUENCE 356 AA; 40067 MW; C75E113BE2A82A8B CRC64;
MTSVTRSEII DEKGPVMSKT HDHQLESSLS PVEVFAKTSA SLEMNQGVSE ERIHLGSSPK
KGGNCDLSHQ ERLQSKSLHL SPQEQSASYQ DRRQSWRRAS MKETNRRKSL HPIHQGITEL
SRSISVDLAE SKRLGCLLLS SFQFSIQKLE PFLRDTKGFS LESFRAKASS LSEELKHFAD
GLETDGTLQK CFEDSNGKAS DFSLEASVAE MKEYITKFSL ERQTWDQLLL HYQQEAKEIL
SRGSTEAKIT EVKVEPMTYL GSSQNEVLNT KPDYQKILQN QSKVFDCMEL VMDELQGSVK
QLQAFMDEST QCFQKVSVQL GKRSMQQLDP SPARKLLKLQ LQNPPAIHGS GSGSCQ
